KAD1_RAT
ID KAD1_RAT Reviewed; 194 AA.
AC P39069; Q5EBC5; Q9JJN3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN Name=Ak1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Noma T.;
RT "Rat adenylate kinase isozyme 1.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 10-21; 32-44; 64-77; 84-97; 101-128; 156-167 AND
RP 172-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-194.
RX PubMed=8468325; DOI=10.1093/oxfordjournals.jbchem.a124026;
RA Tanabe T., Yamada M., Noma T., Kajii T., Nakazawa A.;
RT "Tissue-specific and developmentally regulated expression of the genes
RT encoding adenylate kinase isozymes.";
RL J. Biochem. 113:200-207(1993).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Also displays broad nucleoside diphosphate
CC kinase activity. Plays an important role in cellular energy homeostasis
CC and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_03171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03171}.
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DR EMBL; AB022701; BAA97655.1; -; mRNA.
DR EMBL; BC089797; AAH89797.1; -; mRNA.
DR EMBL; D13376; BAA02643.1; -; mRNA.
DR PIR; PQ0534; PQ0534.
DR RefSeq; NP_077325.2; NM_024349.3.
DR AlphaFoldDB; P39069; -.
DR SMR; P39069; -.
DR BioGRID; 246373; 2.
DR IntAct; P39069; 5.
DR MINT; P39069; -.
DR BindingDB; P39069; -.
DR ChEMBL; CHEMBL3773; -.
DR iPTMnet; P39069; -.
DR PhosphoSitePlus; P39069; -.
DR SwissPalm; P39069; -.
DR jPOST; P39069; -.
DR PRIDE; P39069; -.
DR Ensembl; ENSRNOT00000091048; ENSRNOP00000074303; ENSRNOG00000049056.
DR GeneID; 24183; -.
DR KEGG; rno:24183; -.
DR CTD; 203; -.
DR RGD; 2076; Ak1.
DR GeneTree; ENSGT00940000158325; -.
DR InParanoid; P39069; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; P39069; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:P39069; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0001520; C:outer dense fiber; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0030017; C:sarcomere; IDA:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0046083; P:adenine metabolic process; NAS:RGD.
DR GO; GO:0006172; P:ADP biosynthetic process; IDA:RGD.
DR GO; GO:0046033; P:AMP metabolic process; IDA:RGD.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0046103; P:inosine biosynthetic process; IDA:RGD.
DR GO; GO:0007517; P:muscle organ development; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; IEP:RGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IMP:RGD.
DR GO; GO:0014042; P:positive regulation of neuron maturation; IEP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR HAMAP; MF_03171; Adenylate_kinase_AK1; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR028582; AK1.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158914"
FT REGION 38..67
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT REGION 131..141
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 65..67
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 94..97
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 138
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 149
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P00568, ECO:0000255|HAMAP-
FT Rule:MF_03171"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT CONFLICT 81
FT /note="L -> F (in Ref. 1; BAA97655)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> S (in Ref. 4; BAA02643)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> L (in Ref. 4; BAA02643)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> W (in Ref. 4; BAA02643)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="C -> S (in Ref. 1; BAA97655 and 4; BAA02643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21584 MW; 4D53BCB3EF8B7629 CRC64;
MEDKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SSRGKMLSSI
MEKGELVPLE TVLDMLRDAM LAKVDSSNGF LIDGYPREVK QGEEFERKIA QPTLLLYVDA
GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV ISFYDKRGIV RKVNAEGSVD
TVFSQVCTYL DSLK
